2016
DOI: 10.1038/ncomms13339
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Chaperone addiction of toxin–antitoxin systems

Abstract: Bacterial toxin–antitoxin (TA) systems, in which a labile antitoxin binds and inhibits the toxin, can promote adaptation and persistence by modulating bacterial growth in response to stress. Some atypical TA systems, known as tripartite toxin–antitoxin–chaperone (TAC) modules, include a molecular chaperone that facilitates folding and protects the antitoxin from degradation. Here we use a TAC module from Mycobacterium tuberculosis as a model to investigate the molecular mechanisms by which classical TAs can be… Show more

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Cited by 45 publications
(74 citation statements)
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“…In the majority of cases (33)(34)(35)(36)(37), the Tn3-associated TA gene pairs are located directly upstream of the resolvase genes (tnpR or tnpI) (Fig. S2).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…In the majority of cases (33)(34)(35)(36)(37), the Tn3-associated TA gene pairs are located directly upstream of the resolvase genes (tnpR or tnpI) (Fig. S2).…”
Section: Resultsmentioning
confidence: 99%
“…For TnSku1, the TA genes are located downstream of and expressed toward tnpR, while in the partial copy, TnAmu2_p, there is a short ORF between the divergently transcribed antitoxin and tnpR genes. This does not appear to be related to the 3-component toxin-antitoxin-chaperone (TAC) systems (33).…”
Section: Discussionmentioning
confidence: 98%
“…These studies involved various enzyme families such as RNAses (Christensen & Gerdes, 2003;Kamada et al, 2003;Kamada & Hanaoka, 2005;Winther & Gerdes, 2011), kinases (Castro-Roa et al, 2013;Kaspy et al, 2013;Mutschler et al, 2011), ADP-ribosyl transferases (Jankevicius et al, 2016), acetyltransferases (Cheverton et al, 2016;Jurė nas, Chatterjee et al, 2017) and adenylyltransferases (Engel et al, 2012). In addition, the different mechanisms of toxin neutralization and transcription autoregulation show that the intrinsically disordered regions present in TA antitoxins constitute an important feature of type II TA modules (Bordes et al, 2016;De Gieter et al, 2014;Garcia-Pino, Balasubramanian et al, 2010;Garcia-Pino et al, 2016; beyond providing a target for protease degradation. The toxin AtaT from the ataRT TA module found in enteropathogenic E. coli, Enterobacter, Citrobacter and other bacteria (Jurė nas, Garcia-Pino et al, 2017) was recently described as a member of the GNAT family of N-acetyltransferases.…”
Section: Discussionmentioning
confidence: 99%
“…Analysis of the TAC sequence has revealed that the carboxy terminus of the antitoxin contains an extended chaperone addition sequence, ChAD, that can effectively prevent folding of the antitoxin and specifically recruit the SecB-like chaperone. Fusion of the HigA ChAD sequence to an irrelevant recombinant protein or a typical chaperone-independent type II TA system causes chaperone activity towards these proteins, indicating that the ChAD motif in the antitoxin is transferable [76]. Many questions remain regarding the interaction between the TAS system and the chaperone protein, including whether TAC systems exist in some common pathogens, such as Staphylococcus aureus, which causes skin infections, and whether these chaperones perform the same function to maintain antitoxin stability.…”
Section: Type II Ta System Proteins Interact With Chaperone Proteins mentioning
confidence: 99%